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| | ==Crystal structure of TRAF1 TRAF domain== | | ==Crystal structure of TRAF1 TRAF domain== |
| - | <StructureSection load='5e1t' size='340' side='right' caption='[[5e1t]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='5e1t' size='340' side='right'caption='[[5e1t]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5e1t]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E1T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E1T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5e1t]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E1T FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5e1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e1t OCA], [http://pdbe.org/5e1t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e1t RCSB], [http://www.ebi.ac.uk/pdbsum/5e1t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e1t ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5e1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e1t OCA], [https://pdbe.org/5e1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e1t RCSB], [https://www.ebi.ac.uk/pdbsum/5e1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e1t ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TRAF1_HUMAN TRAF1_HUMAN]] Adapter molecule that regulates the activation of NF-kappa-B and JNK. Plays a role in the regulation of cell survival and apoptosis. The heterotrimer formed by TRAF1 and TRAF2 is part of a E3 ubiquitin-protein ligase complex that promotes ubiquitination of target proteins, such as MAP3K14. The TRAF1/TRAF2 complex recruits the antiapoptotic E3 protein-ubiquitin ligases BIRC2 and BIRC3 to TNFRSF1B/TNFR2.<ref>PMID:10692572</ref> <ref>PMID:16323247</ref> <ref>PMID:18429822</ref> <ref>PMID:19698991</ref> <ref>PMID:19287455</ref> <ref>PMID:20385093</ref> | + | [https://www.uniprot.org/uniprot/TRAF1_HUMAN TRAF1_HUMAN] Adapter molecule that regulates the activation of NF-kappa-B and JNK. Plays a role in the regulation of cell survival and apoptosis. The heterotrimer formed by TRAF1 and TRAF2 is part of a E3 ubiquitin-protein ligase complex that promotes ubiquitination of target proteins, such as MAP3K14. The TRAF1/TRAF2 complex recruits the antiapoptotic E3 protein-ubiquitin ligases BIRC2 and BIRC3 to TNFRSF1B/TNFR2.<ref>PMID:10692572</ref> <ref>PMID:16323247</ref> <ref>PMID:18429822</ref> <ref>PMID:19698991</ref> <ref>PMID:19287455</ref> <ref>PMID:20385093</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | TNF-receptor associated factor (TRAF) proteins are key adaptor molecules containing E3 ubiquitin ligase activity that play a critical role in immune cell signaling. TRAF1 is a unique family of TRAF lacking the N-terminal RING finger domain. TRAF1 is an important scaffold protein that participates in TNFR2 signaling in T cells as a negative or positive regulator via direct interaction with TRAF2, which has recently been identified as a pro-apoptotic regulator in neuronal cell death. Here, we report the first crystal structure of the TRAF1 TRAF domain containing both the TRAF-N coiled-coil domain and the TRAF-C domain. Our structure reveals both similarities and differences with other TRAF family members, which may be functionally relevant to TRAFs. We also found that the TRAF-N coiled-coil domain of TRAF1 is critical for the trimer formation and stability of the protein. Finally, we found that conserved surface residues on the TRAF1 TRAF domain that might be binding hot spots that are critical for interaction with signaling molecules.
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| - | Crystal structure of TRAF1 TRAF domain and its implications in the TRAF1-mediated intracellular signaling pathway.,Kim CM, Choi JY, Bhat EA, Jeong JH, Son YJ, Kim S, Park HH Sci Rep. 2016 May 6;6:25526. doi: 10.1038/srep25526. PMID:27151821<ref>PMID:27151821</ref>
| + | ==See Also== |
| - | | + | *[[TNF receptor-associated factor 3D structures|TNF receptor-associated factor 3D structures]] |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5e1t" style="background-color:#fffaf0;"></div>
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Kim, C M]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Park, H H]] | + | [[Category: Large Structures]] |
| - | [[Category: Protein binding]] | + | [[Category: Kim CM]] |
| - | [[Category: Protein interaction domain]] | + | [[Category: Park HH]] |
| Structural highlights
Function
TRAF1_HUMAN Adapter molecule that regulates the activation of NF-kappa-B and JNK. Plays a role in the regulation of cell survival and apoptosis. The heterotrimer formed by TRAF1 and TRAF2 is part of a E3 ubiquitin-protein ligase complex that promotes ubiquitination of target proteins, such as MAP3K14. The TRAF1/TRAF2 complex recruits the antiapoptotic E3 protein-ubiquitin ligases BIRC2 and BIRC3 to TNFRSF1B/TNFR2.[1] [2] [3] [4] [5] [6]
See Also
References
- ↑ Irmler M, Steiner V, Ruegg C, Wajant H, Tschopp J. Caspase-induced inactivation of the anti-apoptotic TRAF1 during Fas ligand-mediated apoptosis. FEBS Lett. 2000 Feb 25;468(2-3):129-33. PMID:10692572
- ↑ Su X, Li S, Meng M, Qian W, Xie W, Chen D, Zhai Z, Shu HB. TNF receptor-associated factor-1 (TRAF1) negatively regulates Toll/IL-1 receptor domain-containing adaptor inducing IFN-beta (TRIF)-mediated signaling. Eur J Immunol. 2006 Jan;36(1):199-206. PMID:16323247 doi:10.1002/eji.200535415
- ↑ Kato T Jr, Gotoh Y, Hoffmann A, Ono Y. Negative regulation of constitutive NF-kappaB and JNK signaling by PKN1-mediated phosphorylation of TRAF1. Genes Cells. 2008 May;13(5):509-20. doi: 10.1111/j.1365-2443.2008.01182.x. PMID:18429822 doi:10.1111/j.1365-2443.2008.01182.x
- ↑ Lavorgna A, De Filippi R, Formisano S, Leonardi A. TNF receptor-associated factor 1 is a positive regulator of the NF-kappaB alternative pathway. Mol Immunol. 2009 Oct;46(16):3278-82. doi: 10.1016/j.molimm.2009.07.029. Epub, 2009 Aug 20. PMID:19698991 doi:10.1016/j.molimm.2009.07.029
- ↑ Wicovsky A, Henkler F, Salzmann S, Scheurich P, Kneitz C, Wajant H. Tumor necrosis factor receptor-associated factor-1 enhances proinflammatory TNF receptor-2 signaling and modifies TNFR1-TNFR2 cooperation. Oncogene. 2009 Apr 16;28(15):1769-81. doi: 10.1038/onc.2009.29. Epub 2009 Mar 16. PMID:19287455 doi:10.1038/onc.2009.29
- ↑ Zheng C, Kabaleeswaran V, Wang Y, Cheng G, Wu H. Crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 complexes: affinity, specificity, and regulation. Mol Cell. 2010 Apr 9;38(1):101-13. PMID:20385093 doi:10.1016/j.molcel.2010.03.009
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